TFDF_DELAC
ID TFDF_DELAC Reviewed; 352 AA.
AC Q93T12;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Maleylacetate reductase;
DE EC=1.3.1.32;
DE AltName: Full=Chloromaleylacetate reductase;
GN Name=tfdF;
OS Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=80866 {ECO:0000312|EMBL:AAK57010.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=P4a {ECO:0000312|EMBL:AAK57010.2};
RX PubMed=12949179; DOI=10.1099/mic.0.26260-0;
RA Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W.;
RT "A transposon encoding the complete 2,4-dichlorophenoxyacetic acid
RT degradation pathway in the alkalitolerant strain Delftia acidovorans P4a.";
RL Microbiology 149:2545-2556(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-235.
RC STRAIN=P4a {ECO:0000312|EMBL:AAK57010.2};
RA Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W.;
RT "Development and application of PCR primers for the detection of the tfd
RT genes in Delftia acidovorans P4a involved in the degradation of 2,4-D.";
RL Acta Biotechnol. 21:321-331(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-15.
RC STRAIN=MC1;
RX PubMed=15073309; DOI=10.1099/mic.0.26774-0;
RA Benndorf D., Davidson I., Babel W.;
RT "Regulation of catabolic enzymes during long-term exposure of Delftia
RT acidovorans MC1 to chlorophenoxy herbicides.";
RL Microbiology 150:1005-1014(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxoadipate + NAD(+) = H(+) + maleylacetate + NADH;
CC Xref=Rhea:RHEA:16981, ChEBI:CHEBI:15378, ChEBI:CHEBI:15775,
CC ChEBI:CHEBI:16468, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.32;
CC Evidence={ECO:0000250|UniProtKB:P27101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxoadipate + NADP(+) = H(+) + maleylacetate + NADPH;
CC Xref=Rhea:RHEA:16985, ChEBI:CHEBI:15378, ChEBI:CHEBI:15775,
CC ChEBI:CHEBI:16468, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.32;
CC Evidence={ECO:0000250|UniProtKB:P27101};
CC -!- PATHWAY: Aromatic compound metabolism; 3-chlorocatechol degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P94135, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AY078159; AAK57010.2; -; Genomic_DNA.
DR RefSeq; WP_011255148.1; NC_019283.1.
DR RefSeq; YP_006961879.1; NC_019283.1.
DR AlphaFoldDB; Q93T12; -.
DR SMR; Q93T12; -.
DR UniPathway; UPA00083; -.
DR PRO; PR:Q93T12; -.
DR GO; GO:0018506; F:maleylacetate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08177; MAR; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR034786; MAR.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD;
KW Oxidoreductase.
FT CHAIN 1..352
FT /note="Maleylacetate reductase"
FT /id="PRO_0000087850"
SQ SEQUENCE 352 AA; 37499 MW; C72A9D2671FFFAB3 CRC64;
MNFIHDPLTP RVLFGAGRLQ SLGEELKLLG IRRVLVISTP EQRELANQVA ALIPGSVAGF
FDRATMHVPS QIVDQAASVA RELGVDSYVA PGGGSTIGLA KMLALHSSLP IVAIPTTYAG
SEMTSIYGVT ENELKKTGRD RRVLARTVIY DPELTFGLPT GISVTSGLNA IAHAVEGLYA
PEVNPILAIM AQQGIAALAK SIPTIRSAPT DLEARSQAQY GAWLCGSVLG NVSMALHHKL
CHTLGGTFNL PHAETHTVVL PHALAYNTPA IPRANAWLQE ALATREPAQA LFDLAKSNGA
PVSLQSIGMK EADLDRACEL VMSAQYPNPR PLEKHAIANL LRRAYLGEPP QP
